[Amino acid composition, heterogeneity and antiheparin activity of protamine sulfate from the milt roe of the sturgeon Acipenser sturio].
Identifieur interne : 002773 ( Main/Merge ); précédent : 002772; suivant : 002774[Amino acid composition, heterogeneity and antiheparin activity of protamine sulfate from the milt roe of the sturgeon Acipenser sturio].
Auteurs : I N Borodinskaia ; I F MishuninSource :
- Ukrainskii biokhimicheskii zhurnal (1978) [ 0201-8470 ]
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Amino Acids, Protamines.
- analysis : Spermatozoa.
- metabolism : Fishes.
- chemical , pharmacology : Protamines.
- Animals, Chromatography, Ion Exchange, Heparin Antagonists, Male.
Abstract
The homogeneous preparation of protamine sulphate is obtained chromatographically and electrophoretically from milt roe of the sturgeon. Its amino acid composition and properties are studied. The methods to blockade the functional groups of protamine sulphate amino acids is used to investigate the possible mechanism of heparin inactivation.
PubMed: 2631325
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pubmed:2631325Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">[Amino acid composition, heterogeneity and antiheparin activity of protamine sulfate from the milt roe of the sturgeon Acipenser sturio].</title>
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<term>Heparin Antagonists</term>
<term>Male</term>
<term>Protamines (analysis)</term>
<term>Protamines (pharmacology)</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term>
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<front><div type="abstract" xml:lang="en">The homogeneous preparation of protamine sulphate is obtained chromatographically and electrophoretically from milt roe of the sturgeon. Its amino acid composition and properties are studied. The methods to blockade the functional groups of protamine sulphate amino acids is used to investigate the possible mechanism of heparin inactivation.</div>
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